MolNFT v1 · #189108 · protein + RNA
T.THERMOPHILUS 30S ribosome with ksga, class K4
7V2O: “T.THERMOPHILUS 30S ribosome with ksga, class K4”. Electron microscopy, 1 ligand (ZN). MolNFT v1 #189108 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7V2O
- Type
- protein + RNA
- Length
- 4,111 residues
- Chains
- 22
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P80371, P80372, P80373, Q5SHQ5, Q5SLP8, P17291, P0DOY9, P80374, Q5SHN7, P80376, Q5SHN3, P80377, P0DOY6, Q5SJ76, Q5SJH3, P0DOY7, Q5SLQ0, Q5SHP2, P80380, P37468, Q5SIH3
- Ligands
- ZN
Structure
electron microscopy · 22 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | rna | 1487 | — | — |
| B | — | protein | 220 | — | P80371 |
| C | — | protein | 206 | — | P80372 |
| D | — | protein | 208 | — | P80373 |
| E | — | protein | 150 | — | Q5SHQ5 |
| F | — | protein | 101 | — | Q5SLP8 |
| G | — | protein | 155 | — | P17291 |
| H | — | protein | 138 | — | P0DOY9 |
| I | — | protein | 127 | — | P80374 |
| J | — | protein | 98 | — | Q5SHN7 |
| K | — | protein | 119 | — | P80376 |
| L | — | protein | 124 | — | Q5SHN3 |
| M | — | protein | 113 | — | P80377 |
| N | — | protein | 60 | — | P0DOY6 |
| O | — | protein | 88 | — | Q5SJ76 |
| P | — | protein | 81 | — | Q5SJH3 |
| Q | — | protein | 100 | — | P0DOY7 |
| R | — | protein | 69 | — | Q5SLQ0 |
| S | — | protein | 80 | — | Q5SHP2 |
| T | — | protein | 99 | — | P80380 |
| U | — | protein | 264 | — | P37468 |
| V | — | protein | 24 | — | Q5SIH3 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains D, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7V2O · T.thermophilus 30S ribosome with KsgA, class K4 · the same entry in another collection · chain V against V, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P80371
- Every structure of UniProt P80372
- Every structure of UniProt P80373
- Every structure of UniProt Q5SHQ5
- Every structure of UniProt Q5SLP8
- Every structure of UniProt P17291
- Every structure of UniProt P0DOY9
- Every structure of UniProt P80374
- Every structure of UniProt Q5SHN7
- Every structure of UniProt P80376
- Every structure of UniProt Q5SHN3
- Every structure of UniProt P80377
- Every structure of UniProt P0DOY6
- Every structure of UniProt Q5SJ76
- Every structure of UniProt Q5SJH3
- Every structure of UniProt P0DOY7
- Every structure of UniProt Q5SLQ0
- Every structure of UniProt Q5SHP2
- Every structure of UniProt P80380
- Every structure of UniProt P37468
- Every structure of UniProt Q5SIH3
- Elsewhere: RCSB PDB 7V2O · PDBe 7V2O · UniProt P80371 · UniProt P80372 · UniProt P80373 · UniProt Q5SHQ5 · UniProt Q5SLP8 · UniProt P17291 · UniProt P0DOY9 · UniProt P80374 · UniProt Q5SHN7 · UniProt P80376 · UniProt Q5SHN3 · UniProt P80377 · UniProt P0DOY6 · UniProt Q5SJ76 · UniProt Q5SJH3 · UniProt P0DOY7 · UniProt Q5SLQ0 · UniProt Q5SHP2 · UniProt P80380 · UniProt P37468 · UniProt Q5SIH3
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